{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haase A"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["341-351"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9900092"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(2)"],"pubmed_abstract":["Four Hyp proteins build a scaffold complex upon which the Fe(CN)<sub>2</sub> CO group of the [NiFe]-cofactor of hydrogenases (Hyd) is made. Two of these Hyp proteins, the redox-active, [4Fe-4S]-containing HypD protein and the HypC chaperone, form the basis of this scaffold complex. Two different scaffold complexes exist in Escherichia coli, HypCD, and the paralogous HybG-HypD complex, both of which exhibit ATPase activity. Apart from a Rossmann fold, there is no obvious ATP-binding site in HypD. The aim of this study, therefore, was to identify amino acid motifs in HypD that are required for the ATPase activity of the HybG-HypD scaffold complex. Amino acid-exchange variants in three conserved motifs within HypD were generated. Variants in which individual cysteine residues coordinating the"],"journal":["FEBS open bio"],"pubmed_title":["A redox-active HybG-HypD scaffold complex is required for optimal ATPase activity during [NiFe]-hydrogenase maturation in Escherichia coli."],"pmcid":["PMC9900092"],"funding_grant_id":["SA 494/7‐2","SPP 1927"],"pubmed_authors":["Sawers RG","Haase A"],"additional_accession":[]},"is_claimable":false,"name":"A redox-active HybG-HypD scaffold complex is required for optimal ATPase activity during [NiFe]-hydrogenase maturation in Escherichia coli.","description":"Four Hyp proteins build a scaffold complex upon which the Fe(CN)<sub>2</sub> CO group of the [NiFe]-cofactor of hydrogenases (Hyd) is made. Two of these Hyp proteins, the redox-active, [4Fe-4S]-containing HypD protein and the HypC chaperone, form the basis of this scaffold complex. Two different scaffold complexes exist in Escherichia coli, HypCD, and the paralogous HybG-HypD complex, both of which exhibit ATPase activity. Apart from a Rossmann fold, there is no obvious ATP-binding site in HypD. The aim of this study, therefore, was to identify amino acid motifs in HypD that are required for the ATPase activity of the HybG-HypD scaffold complex. Amino acid-exchange variants in three conserved motifs within HypD were generated. Variants in which individual cysteine residues coordinating the","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-05-28T18:36:47.368Z","creation":"2025-04-07T13:01:49.356Z"},"accession":"S-EPMC9900092","cross_references":{"pubmed":["36602404"],"doi":["10.1002/2211-5463.13546"]}}